1dps
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THE CRYSTAL STRUCTURE OF DPS, A FERRITIN HOMOLOG THAT BINDS AND PROTECTS DNA
OverviewOverview
The crystal structure of Dps, a DNA-binding protein from starved E. coli, that protects DNA from oxidative damage, has been solved at 1.6 A, resolution. The Dps monomer has essentially the same fold as ferritin, which forms a 24-mer with 432 symmetry, a hollow core and pores at the, three-fold axes. Dps forms a dodecamer with 23 (tetrahedral) point group, symmetry which also has a hollow core and pores at the three-folds. The, structure suggests a novel DNA-binding motif and a mechanism for DNA, protection based on the sequestration of Fe ions.
About this StructureAbout this Structure
1DPS is a Single protein structure of sequence from Escherichia coli with NA as ligand. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of Dps, a ferritin homolog that binds and protects DNA., Grant RA, Filman DJ, Finkel SE, Kolter R, Hogle JM, Nat Struct Biol. 1998 Apr;5(4):294-303. PMID:9546221
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